Abnormal protein deposits in the brain which contain fibrilized forms of Abeta and alpha-synuclein proteins are characteristic of Alzheimer's Disease and Parkinson's Disease, and they may play a causative role in neurodegeneration. Detailed knowledge of the aggregation mechanisms of Abeta and alpha-synuclein would elucidate the steps in disease progression, potentially identifying therapeutic strategies. The proposed research will continue a scanning force microscopy (SFM) study of Abeta and initiate similar research on alpha-synuclein. The SFM studies will use recently developed carbon nanotube tips, which allow higher resolution imaging than previously attained. Chemical force microscopy (CFM) with nanotube tips will be used to map the functional group distribution on the protein aggregates with high resolution. Concurrently, the further sharpening of nanotube tips will be pursued by sputtering and electrochemical etching techniques. The ultimate goal, a tip which ends in an individual singe-walled nanotube, should achieve 1 - 2 nm resolution in SFM and CFM, an order of magnitude improvement over standard SFM tips. These ultrahigh resolution tips will be used to achieve a molecular scale understanding of Abeta and alpha-synuclein aggregation.